Immuno-informatics Characterization SARS-CoV-2 Spike Glycoprotein for Prioritization of Epitope based Multivalent Peptide Vaccine

Saba Ismail; Sajjad Ahmad; Syed Sikander Azam

The net free energy of the simulated system was subjected to per residues and pairwise residues decomposition to point residues that contribute majorly in system stabilization and lower energy. Molecular docking simulation studies demonstrated 64 residues from the TLR3 receptor that are in direct contact with the MEPVC but per residue decomposition assay illustrated that among the residues only Hie31, Phe55, Glu98, Hie100, Met102, Ile121, Thr122, Asp124, Glu146, Glu146, Glu174, Ser176, Phe198, Asn200, Ser225, Met249, Asp251, Tyr254, Tyr273, Phe275, Tyr278, Tyr297, Glu323, Hie324, and Tyr348 are hotspot as they contribute rigoursly in binding interaction with MEPVC at the docked side. The side chain of Hie100, Thr122, Asp124, Glu174, Ser176, Tyr254, and Glu323 contribute significantly in chemical interactions and have energy value in following order: -2.86602 kcal/mol, -3.71782 kcal/mol, -3.77019 kcal/mol, -3.80724 kcal/mol, -2.71475 kcal/mol, -2.40187 kcal/mol, and -3.54158 kcal/mol, respectively. To these TLR3 hotspot residues, the MEPVC interacting residues were also observed in quite lower energies illustrating high affinity for the receptor residues for chemical interactions.